ID A0A1G4BLL8_9PEZI Unreviewed; 599 AA.
AC A0A1G4BLL8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN ORFNames=CORC01_02297 {ECO:0000313|EMBL:OHF02304.1};
OS Colletotrichum orchidophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=1209926 {ECO:0000313|EMBL:OHF02304.1, ECO:0000313|Proteomes:UP000176998};
RN [1] {ECO:0000313|EMBL:OHF02304.1, ECO:0000313|Proteomes:UP000176998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 309357 {ECO:0000313|EMBL:OHF02304.1,
RC ECO:0000313|Proteomes:UP000176998};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary aliphatic amine + H2O + O2 = a primary amine + an
CC aldehyde + H2O2; Xref=Rhea:RHEA:26414, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478,
CC ChEBI:CHEBI:58855, ChEBI:CHEBI:65296; EC=1.4.3.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000205};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362067};
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995, ECO:0000256|RuleBase:RU362067}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OHF02304.1}.
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DR EMBL; MJBS01000013; OHF02304.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4BLL8; -.
DR STRING; 1209926.A0A1G4BLL8; -.
DR OrthoDB; 5471885at2759; -.
DR Proteomes; UP000176998; Unassembled WGS sequence.
DR GO; GO:0097621; F:monoamine oxidase activity; IEA:RHEA.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR Gene3D; 3.30.1330.40; RutC-like; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR InterPro; IPR035959; RutC-like_sf.
DR InterPro; IPR006175; YjgF/YER057c/UK114.
DR PANTHER; PTHR43563; AMINE OXIDASE; 1.
DR PANTHER; PTHR43563:SF14; AMINE OXIDASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR Pfam; PF01042; Ribonuc_L-PSP; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55298; YjgF-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU362067};
KW Flavoprotein {ECO:0000256|RuleBase:RU362067};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362067};
KW Reference proteome {ECO:0000313|Proteomes:UP000176998}.
FT DOMAIN 154..587
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 599 AA; 64886 MW; 72D7DEBA203A2F46 CRC64;
MTRLIATVDL SNTGTAYYAP ATITRAGSLV HVSGLPGNTK DGKVPSDYDS QIHLALLNLR
KVIIAAGSTV SNIASLTLYI VDYDASKRQH ARHVQRFLGT HRPAMTLVPV QKLAVPGWLI
EINAVVARPE APPVPRSLPP VQETADVVII GAGLAGLSAA HEVRRAGLSC IVLEARDRVG
GKTWSQPMEG SGDRGVFDLG AAWINDTNQS RMYELAKRYG AELIEQNTNG NCVLQDFDGK
CSPFAYGELP KACSEIRDMA EADCQALDVF RPKDTSLDSL TFEAYLKSRG ADSVALATAT
IWTRAMLGQE PKDISALYFL NYCKSGGGLL QMRSDRKDGG QYLRVRQGTQ LFSKGLASSL
PEGVVRLSNP VQTVVQSENR SVKVEAGGKV YSAQKVITTV PGPVLKTISF QPSLPHTKLA
WIESQTYGYY TKAMMEFSAP FWVEKGFCGL AQSFVGPASV VRDTSSPVDE KFVLTCFLAG
EPGKAWAALT TAQRENGLLE QLSQLYDIEN IRPLFKQMVL YEWVNDEFSG WGCPCTSLGP
GVLDTLGGDG LREPYRDLHF AGTETAGEWK GYMEGAVRSG ERAGAEVVKS LNGGIVSRL
//
